Stability of the residual structure in unfolded BPTI in different conditions of temperature and solvent composition measured by disulphide kinetics and double mutant cycle analysis.

Abstract excerpt

The folding funnel model proposes a clear description of the protein folding process. To test this model, additional data on the structures populated in different stages of folding and their influence on further folding are required. Here, we use the double mutant strategy and disulphide formation kinetics measurements to study the impact on folding of the residual structure in unfolded bovine pancreatic trypsin...

Topics

• Animals
• Aprotinin
• Cattle
• Cysteine
• Disulfides
• Glutathione Disulfide
• Guanidine
• Kinetics
• Models, Molecular
• Mutation
• Osmolar Concentration